› 5i7l

X-ray diffraction
2.6Å resolution

Crystal Structure of SPLUNC1 Disulfide Mutant M2 (A48C, V253C)

Released:
DOI: 10.2210/pdb5i7l/pdb
PDB entry 5i7l coloured by chain, front view.
PDB entry 5i7l coloured by chain, side view.
PDB entry 5i7l coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural Features Essential to the Antimicrobial Functions of Human SPLUNC1.
Walton WG, Ahmad S, Little MS, Kim CS, Tyrrell J, Lin Q, Di YP, Tarran R, Redinbo MR
Biochemistry 55 2979-91 (2016)
PMID: 27145151

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-192446 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
BPI fold-containing family A member 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 240 amino acids
Theoretical weight: 25 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9NP55 (Residues: 19-256; Coverage: 100%)
Gene names: BPIFA1, LUNX, NASG, PLUNC, SPLUNC1, SPURT, UNQ787/PRO1606
Sequence domains: LBP / BPI / CETP family, N-terminal domain
Structure domains: Bactericidal permeability-increasing protein; domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: C2221
Unit cell:
a: 47.083Å b: 203.588Å c: 120.211Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.226 0.22 0.284
Expression system: Escherichia coli

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Citations

7 review citations

pH Dependent Antimicrobial Peptides and Proteins, Their Mechanisms of Action and Potential as Therapeutic Agents.
Malik et al. (2016)
6 more